Light‐driven biocatalysis with cytochrome P450 peroxygenases. (25th January 2013)

• Record Type: Journal Article
• Authors: Girhard, Marco; Kunigk, Elmar; Tihovsky, Svetlana; Shumyantseva, Victoria V.; Urlacher, Vlada B.; Gilardi, Gianfranco
• Is Part Of: Biotechnology and applied biochemistry. Volume 60:Number 1(2013:Jan./Feb.)
• Page Start: 111
• Page End: 118
• Publication Date: 2013-01-25
• Subjects: Biotechnology -- Periodicals; Biochemical engineering -- Periodicals; Biochemistry -- Periodicals; Biochemistry -- Periodicals; Genetic Techniques -- Periodicals; Microbiological Techniques -- Periodicals; 660.6
• DOI: 10.1002/bab.1063
• Languages: English
• ISSNs: 0885-4513

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>The cytochrome P450 peroxygenases P450_Bsβ (CYP152A1) from <italic>Bacillus subtilis</italic> and P450_Cla (CYP152A2) from <italic>Clostridium acetobutylicum</italic> belong to a unique group of P450s with high synthetic potential. They consume hydrogen peroxide via the peroxide shunt and therefore do not require additional electron transfer proteins for biocatalytic activity. Their high synthetic potential is, however, impaired by their rather poor operational stability in the presence of hydrogen peroxide. Herein, we report the use of a light‐driven approach utilizing light‐excited flavins (riboflavin, flavin mononucleotide, or flavin adenine dinucleotide) and the electron donor ethylenediaminetetraacetate as the electron source for the <italic>in situ</italic> generation of hydrogen peroxide. This approach represents a simple and easily applicable way to promote oxyfunctionalization reactions catalyzed by P450 peroxygenases and is useful for biocatalysis with these enzymes.</p> </abstract>